PMID: 1187571Sep 1, 1975Paper

Isolation and some properties of a nonspecific extracellular ribonuclease of Aspergillus clavatus

Prikladnaia biokhimiia i mikrobiologiia
G S Ivanova, L K Grunina


RNase has been isolated from the homogenate of the Aspergillus clavatus mycelium by gel filtration through Sephadex G-75, chromatography on CM-cellulose and DEAE-cellulose. By gel filtration and electrophoresis in polyacrylamide gel the preparation has been shown to be homogeneous. The enzyme is acid protein with the isoelectric point at pH 4.4 and molecular weight of 27,000. RNase has pH optimum at 6.0--6.2 and temperature optimum 60 degrees for RNA action. The enzyme splits RNA completely in the absence of metal ions. Ions Zn2+, Cu+2, Ag+1 and Ni+2 at a concentration of 10(-4) M are strong inhibitors of RNase activity.

Related Concepts

Chromatography, DEAE-Cellulose
Molecular Sieve Chromatography
Ion-Exchange Chromatography Procedure
Enzyme Activation
Isoelectric Point
Alkaline Ribonuclease

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